Plant Physiol.
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Plant Physiology 49:293-298 (1972)
© 1972 American Society of Plant Biologists

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Articles

A Cell Wall-degrading Endopolygalacturonase Secreted by Colletotrichum lindemuthianum1

Patricia D. English, Austin Maglothin, Kenneth Keegstra2 and Peter Albersheim

a Department of Chemistry, University of Colorado, Boulder, Colorado 80302

Cultures of Colletotrichum lindemuthianum (Saccardo and Magnus) Scribner have been induced to secrete an endopolygalacturonase (polygalacturonide glycanohydrolase EC3.2. 1.15). This enzyme has been brought to a high state of purity by ion exchange, gel filtration, and agarose affinity chromatography. The enzyme has optimal activity at pH 5, has an apparent molecular weight as determined by gel filtration of about 70,000, and prefers polygalacturonic acid to pectin as its substrate. The enzyme, while hydrolyzing only 1% of the glycosidic bonds, reduces the viscosity of a polygalacturonic solution by 50%. Nevertheless, the initial as well as the final products of polygalacturonic acid hydrolysis are predominantly tri- and digalacturonic acid and, to a lesser extent, monogalacturonic acid. The purified enzyme catalyzes the removal of about 80% of the galacturonic acid residues of cell walls isolated from suspension-cultured sycamore cells (Acer pseudoplatanus) as well as from the walls isolated from 8-day-old Red Kidney bean (Phaseolus vulgaris) hypocotyls.

2 Recipient of a National Institutes of Health Predoctoral Fellowship.

1 This research was supported by United States Atomic Energy Commission Grant AT(11-1)-1426 and by a University of Colorado Faculty Fellowship.






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